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1BMD

DETERMINANTS OF PROTEIN THERMOSTABILITY OBSERVED IN THE 1.9 ANGSTROMS CRYSTAL STRUCTURE OF MALATE DEHYDROGENASE FROM THE THERMOPHILIC BACTERIUM THERMUS FLAVUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006099biological_processtricarboxylic acid cycle
A0006107biological_processoxaloacetate metabolic process
A0006108biological_processmalate metabolic process
A0006734biological_processNADH metabolic process
A0016491molecular_functionoxidoreductase activity
A0016615molecular_functionmalate dehydrogenase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0030060molecular_functionL-malate dehydrogenase (NAD+) activity
B0003824molecular_functioncatalytic activity
B0006099biological_processtricarboxylic acid cycle
B0006107biological_processoxaloacetate metabolic process
B0006108biological_processmalate metabolic process
B0006734biological_processNADH metabolic process
B0016491molecular_functionoxidoreductase activity
B0016615molecular_functionmalate dehydrogenase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0030060molecular_functionL-malate dehydrogenase (NAD+) activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NAD A 334
ChainResidue
AGLY10
AGLN111
AVAL128
AGLY129
AASN130
AMET154
AHIS186
AHOH342
AHOH356
AHOH430
AGLY13
AGLN14
AILE15
AGLU41
AILE42
AVAL86
AGLY87
AALA88

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE NAD B 334
ChainResidue
BGLY10
BGLY13
BGLN14
BILE15
BLEU40
BGLU41
BILE42
BVAL86
BGLY87
BALA88
BGLN111
BVAL128
BGLY129
BASN130
BMET154
BHIS186
BHOH345
BHOH357
BHOH437
BHOH491

Functional Information from PROSITE/UniProt
site_idPS00068
Number of Residues13
DetailsMDH Malate dehydrogenase active site signature. MTRLDhnRAkaqL
ChainResidueDetails
AMET154-LEU166

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AHIS186
BHIS186

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341, ECO:0000269|PubMed:8471603
ChainResidueDetails
AGLY10
AVAL128
BGLY10
BVAL128

site_idSWS_FT_FI3
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517
ChainResidueDetails
AARG91
BARG161
AARG97
AASN104
AASN130
AARG161
BARG91
BARG97
BASN104
BASN130

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01517, ECO:0000269|PubMed:16009341
ChainResidueDetails
AGLN111
BGLN111

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AASN185
AASP158

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BASN185
BASP158

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
AHIS186
AARG161
AASP158

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1emd
ChainResidueDetails
BHIS186
BARG161
BASP158

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PDB entries from 2024-07-17

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